Identification of a serine protease inhibitor which causes inclusion vacuole reduction and is lethal to Chlamydia trachomatis.
about
Applications of small molecule probes in dissecting mechanisms of bacterial virulence and host responsesProgress and prospects for small-molecule probes of bacterial imaging.A Chlamydia trachomatis strain with a chemically generated amino acid substitution (P370L) in the cthtrA gene shows reduced elementary body production.Chemoproteomic profiling of host and pathogen enzymes active in choleraCharacterisation of worldwide Helicobacter pylori strains reveals genetic conservation and essentiality of serine protease HtrA.Chlamydia Serine Protease Inhibitor, targeting HtrA, as a New Treatment for Koala Chlamydia infection.HtrA-mediated E-cadherin cleavage is limited to DegP and DegQ homologs expressed by gram-negative pathogensCtHtrA: the lynchpin of the chlamydial surface and a promising therapeutic target.The protease inhibitor JO146 demonstrates a critical role for CtHtrA for Chlamydia trachomatis reversion from penicillin persistence.Overexpression of serine protease HtrA enhances disruption of adherens junctions, paracellular transmigration and type IV secretion of CagA by Helicobacter pylori.Campylobacter jejuni serine protease HtrA plays an important role in heat tolerance, oxygen resistance, host cell adhesion, invasion, and transmigration.The salt-sensitive structure and zinc inhibition of Borrelia burgdorferi protease BbHtrA.Bacterial serine protease HtrA as a promising new target for antimicrobial therapy?Proteases and protease inhibitors in infectious diseases.Amino-Terminal Processing of Helicobacter pylori Serine Protease HtrA: Role in Oligomerization and Activity Regulation.
P2860
Q26822978-EB46AE73-F8E2-4AB9-9120-3C66940765F8Q36055646-3D86954F-111C-40EA-9CD7-3418027DDD94Q36111865-8AFD2FF8-BC3F-4EC3-BC77-718D4EE91056Q36614194-DB8137D9-2008-41F0-9625-F4B98CAEA356Q36800042-3B8CDC56-A964-43EA-9223-7BE912FD5230Q37181409-DDEB3902-7F67-4485-983B-9CFCB71F388EQ37487880-303AFB33-0F46-407B-A46E-25BAF8D69259Q37834000-7E02767D-D651-4881-9ED0-40E8EF53AF82Q37845183-C2E10DB0-DB13-47AC-8357-F45A6D0865D5Q38645512-2F570E30-2694-4E1D-8C6A-8947DFB604C0Q39656118-165F5BBA-F90E-41E8-A78F-4DDD4086F135Q40946216-9B182E82-5CA7-45D2-AE53-975110295E15Q42332065-3CD353BF-C218-4440-9320-58491FF1E689Q47576680-8AC2EFF6-4B9F-4A23-A7BB-651C3DD96286Q52715347-BE8AC9C3-20A6-43B4-84C8-B8D29742565C
P2860
Identification of a serine protease inhibitor which causes inclusion vacuole reduction and is lethal to Chlamydia trachomatis.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 12 July 2013
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Identification of a serine pro ...... thal to Chlamydia trachomatis.
@en
Identification of a serine pro ...... thal to Chlamydia trachomatis.
@nl
type
label
Identification of a serine pro ...... thal to Chlamydia trachomatis.
@en
Identification of a serine pro ...... thal to Chlamydia trachomatis.
@nl
prefLabel
Identification of a serine pro ...... thal to Chlamydia trachomatis.
@en
Identification of a serine pro ...... thal to Chlamydia trachomatis.
@nl
P2093
P2860
P50
P356
P1476
Identification of a serine pro ...... ethal to Chlamydia trachomatis
@en
P2093
James C Powers
John A Allan
Jozef Oleksyszyn
Melisa Merdanovic
Pooja Patel
Sarina Gloeckl
Vanissa A Ong
P2860
P304
P356
10.1111/MMI.12306
P407
P50
P577
2013-07-12T00:00:00Z